GLTP_BACSU
ID GLTP_BACSU Reviewed; 414 AA.
AC P39817;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Proton/glutamate-aspartate symporter {ECO:0000305};
DE AltName: Full=Proton/glutamate symport protein {ECO:0000303|PubMed:7751298};
GN Name=gltP {ECO:0000303|PubMed:7751298}; OrderedLocusNames=BSU02340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / 6GM;
RX PubMed=7751298; DOI=10.1128/jb.177.10.2863-2869.1995;
RA Tolner B., Ubbink-Kok T., Poolman B., Konings W.N.;
RT "Characterization of the proton/glutamate symport protein of Bacillus
RT subtilis and its functional expression in Escherichia coli.";
RL J. Bacteriol. 177:2863-2869(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the proton-dependent, binding-protein-independent
CC transport of glutamate and aspartate. {ECO:0000269|PubMed:7751298}.
CC -!- ACTIVITY REGULATION: Glutamate uptake is inhibited by beta-
CC hydroxyaspartate and cysteic acid. {ECO:0000269|PubMed:7751298}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for glutamate {ECO:0000269|PubMed:7751298};
CC Vmax=65 nmol/min/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:7751298};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7751298};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; U15147; AAA82878.1; -; Genomic_DNA.
DR EMBL; AB006424; BAA33131.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12028.1; -; Genomic_DNA.
DR PIR; B57142; B57142.
DR RefSeq; NP_388116.1; NC_000964.3.
DR RefSeq; WP_003234847.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P39817; -.
DR SMR; P39817; -.
DR STRING; 224308.BSU02340; -.
DR PaxDb; P39817; -.
DR PRIDE; P39817; -.
DR EnsemblBacteria; CAB12028; CAB12028; BSU_02340.
DR GeneID; 938421; -.
DR KEGG; bsu:BSU02340; -.
DR PATRIC; fig|224308.179.peg.240; -.
DR eggNOG; COG1301; Bacteria.
DR InParanoid; P39817; -.
DR OMA; NFVYVIP; -.
DR PhylomeDB; P39817; -.
DR BioCyc; BSUB:BSU02340-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0006835; P:dicarboxylic acid transport; IBA:GO_Central.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..414
FT /note="Proton/glutamate-aspartate symporter"
FT /id="PRO_0000202087"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..42
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..144
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..219
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..300
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 44615 MW; BFF9008FBA4A5298 CRC64;
MKKLIAFQIL IALAVGAVIG HFFPDFGMAL RPVGDGFIRL IKMIVVPIVF STIVIGAAGS
GSMKKMGSLG IKTIIWFEVI TTLVLGLGLL LANVLKPGVG LDLSHLAKKD IHELSGYTDK
VVDFKQMILD IIPTNIIDVM ARNDLLAVIF FAILFGVAAA GIGKASEPVM KFFESTAQIM
FKLTQIVMVT APIGVLALMA ASVGQYGIEL LLPMFKLVGT VFLGLFLILF VLFPLVGLIF
QIKYFEVLKM IWDLFLIAFS TTSTETILPQ LMDRMEKYGC PKRVVSFVVP SGLSLNCDGS
SLYLSVSCIF LAQAFQVDMT LSQQLLMMLV LVMTSKGIAA VPSGSLVVLL ATANAVGLPA
EGVAIIAGVD RVMDMARTGV NVPGHAIACI VVSKWEKAFR QKEWVSANSQ TESI
